Pyruvate carboxylase 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32327 (PYC2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyruvate carboxylase 2
EC=6.4.1.1

Alternative name(s):
Pyruvic carboxylase 2
Short name=PCB 2

Gene names

Name:	PYC2
Ordered Locus Names:	YBR218C
ORF Names:	YBR1507

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1180 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic activity	ATP + pyruvate + HCO₃^- = ADP + phosphate + oxaloacetate.
Cofactor	Biotin. Zinc.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Induction	By glucose.
Miscellaneous	Present with 17000 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Cytoplasm
Ligand	ATP-binding Biotin Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from mutant phenotype PubMed 8185321. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 196563 PubMed 2039506 PubMed 2665820. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate carboxylase activity Inferred from direct assay PubMed 2039506. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1180

1180

Pyruvate carboxylase 2

PRO_0000146825

Regions

Domain

19 – 471

453

Biotin carboxylation

Domain

141 – 338

198

ATP-grasp

Domain

558 – 825

268

Carboxyltransferase

Domain

1102 – 1169

Biotinyl-binding

Region

566 – 570

Substrate binding By similarity

Sites

Active site

313

By similarity

Metal binding

567

Divalent metal cation By similarity

Metal binding

735

Divalent metal cation; via carbamate group By similarity

Metal binding

765

Divalent metal cation By similarity

Metal binding

767

Divalent metal cation By similarity

Binding site

137

ATP By similarity

Binding site

221

ATP By similarity

Binding site

256

ATP By similarity

Binding site

639

Substrate By similarity

Binding site

899

Substrate By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

513

Phosphoserine Ref.6

Modified residue

735

N6-carboxylysine By similarity

Modified residue

1136

N6-biotinyllysine By similarity

Experimental info

Sequence conflict

S → C in CAA42544. Ref.1

Sequence conflict

132

D → E in CAA42544. Ref.1

Sequence conflict

238

N → K in CAA42544. Ref.1

Sequence conflict

268

L → F in CAA42544. Ref.1

Sequence conflict

546

S → C in CAA42544. Ref.1

Sequence conflict

642

N → T in CAA42544. Ref.1

Sequence conflict

771 – 773

GTA → STR in CAA42544. Ref.1

Sequence conflict

831

W → R in CAA42544. Ref.1

Sequence conflict

839

S → P in CAA42544. Ref.1

Sequence conflict

1001

Y → N in CAA42544. Ref.1

Sequence conflict

1155

K → R in CAA42544. Ref.1

Sequence conflict

1178

Q → P in CAA42544. Ref.1

Sequence conflict

1180

K → KVIFTR in CAA42544. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32327 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: AD60DA3A60F5E001
Show »

FASTA

1,180

130,167

        10         20         30         40         50         60 
MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY SHEDRLSMHR 

        70         80         90        100        110        120 
LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH PGYGFLSENS EFADKVVKAG 

       130        140        150        160        170        180 
ITWIGPPAEV IDSVGDKVSA RHLAARANVP TVPGTPGPIE TVQEALDFVN EYGYPVIIKA 

       190        200        210        220        230        240 
AFGGGGRGMR VVREGDDVAD AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG 

       250        260        270        280        290        300 
NVVHLFERDC SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD 

       310        320        330        340        350        360 
NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD KITTRGFSIQ 

       370        380        390        400        410        420 
CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG ATISPHYDSM LVKCSCSGST 

       430        440        450        460        470        480 
YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN 

       490        500        510        520        530        540 
RAQKLLHYLA DLAVNGSSIK GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL 

       550        560        570        580        590        600 
LEKGPSEFAK QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE 

       610        620        630        640        650        660 
CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP DNAIDHFVKQ 

       670        680        690        700        710        720 
AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC YSGDMLQPGK KYNLDYYLEV 

       730        740        750        760        770        780 
VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI GSLRTRYPDL PIHVHSHDSA GTAVASMTAC 

       790        800        810        820        830        840 
ALAGADVVDV AINSMSGLTS QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC 

       850        860        870        880        890        900 
FEADLKGPDP EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP 

       910        920        930        940        950        960 
TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF PEPLRSDVLR 

       970        980        990       1000       1010       1020 
NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS YNMYPRVYED FQKIRETYGD 

      1030       1040       1050       1060       1070       1080 
LSVLPTKNFL APAEPDEEIE VTIEQGKTLI IKLQAVGDLN KKTGQREVYF ELNGELRKIR 

      1090       1100       1110       1120       1130       1140 
VADKSQNIQS VAKPKADVHD THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV 

      1150       1160       1170       1180 
VSSPADGQVK DVFIKDGESV DASDLLVVLE EETLPPSQKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains." Stucka R., Dequin S., Salmon J.-M., Gancedo C. Mol. Gen. Genet. 229:307-315(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects on protein biotinylation." Val D.L., Chapman-Smith A., Walker M.E., Cronan J.E. Jr., Wallace J.C. Biochem. J. 312:817-825(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-513, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59890 Genomic DNA. Translation: CAA42544.1. U35647 Genomic DNA. Translation: AAC49147.1. Z36087 Genomic DNA. Translation: CAA85182.1. BK006936 Genomic DNA. Translation: DAA07334.1.
PIR	S46094.
RefSeq	NP_009777.1. NM_001178566.1.
3D structure databases
ProteinModelPortal	P32327.
SMR	P32327. Positions 22-1170.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6426N.
IntAct	P32327. 4 interactions.
MINT	MINT-2781496.
STRING	4932.YBR218C.
Proteomic databases
PaxDb	P32327.
PeptideAtlas	P32327.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR218C; YBR218C; YBR218C.
GeneID	852519.
KEGG	sce:YBR218C.
Organism-specific databases
CYGD	YBR218c.
SGD	S000000422. PYC2.
Phylogenomic databases
eggNOG	COG1038.
GeneTree	ENSGT00550000074986.
HOGENOM	HOG000282801.
KO	K01958.
OMA	ATNYIGA.
OrthoDB	EOG4578FP.
Enzyme and pathway databases
BRENDA	6.4.1.1. 984.
UniPathway	UPA00138.
Gene expression databases
Genevestigator	P32327.
GermOnline	YBR218C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.10.60. 1 hit. 3.20.20.70. 1 hit. 3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005481. CarbamoylP_synth_lsu_N. IPR003379. Carboxylase_cons_dom. IPR005479. CbamoylP_synth_lsu-like_ATP-bd. IPR009057. Homeodomain-like. IPR016185. PreATP-grasp_dom. IPR000891. PYR_CT. IPR005930. Pyruv_COase. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
PANTHER	PTHR18866:SF10. PTHR18866:SF10. 1 hit.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. PF00682. HMGL-like. 1 hit. PF02436. PYC_OADA. 1 hit. [Graphical view]
PIRSF	PIRSF001594. Pyruv_carbox. 1 hit.
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit. SSF52440. PreATP-grasp-like. 1 hit. SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMs	TIGR01235. pyruv_carbox. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00188. BIOTIN. 1 hit. PS50968. BIOTINYL_LIPOYL. 1 hit. PS50989. COA_CT_CTER. False negative. PS50980. COA_CT_NTER. False negative. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. PS50991. PYR_CT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971553.

Entry information

Entry name

PYC2_YEAST

Accession

Primary (citable) accession number: P32327
Secondary accession number(s): D6VQL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents